Small neutral organic compounds have traditionally the role of markers in 
electrophoresis, as they are expected to have zero electrophoretic mobility 
in external electric fields. The background electrolyte contains, however, 
ions which have unequal affinities to the neutral molecules, which in turn 
results in their mobilization. In this study we focused on two electrophoretic 
markers - thiourea and dimethylsulfoxide, as well as on N-methyl acetamide as 
a model of the peptide bond. By means of capillary electrophoresis and all 
atom molecular dynamics simulations we explored mobilization of these neutral 
compounds in large set of Hofmeister salts. Employing a statistical mechanics 
approach, we were able to reproduce by simulations the experimental electrophoretic 
mobility coefficients. We also established the role of the chemical composition 
of marker and the background electrolyte on the measured electrophoretic mobility 
coefficient. For N-methyl acetamide, we interpreted the results in terms of the 
relative affinities of cations vs. anions to the peptide bond.